UniProtKB - P23583 (MYC_PANTR)
Myc proto-oncogene protein
MYC
Functioni
GO - Molecular functioni
- DNA binding Source: UniProtKB
- DNA-binding transcription activator activity, RNA polymerase II-specific Source: GO_Central
- DNA-binding transcription factor activity Source: UniProtKB
- DNA-binding transcription factor activity, RNA polymerase II-specific Source: UniProtKB
- E-box binding Source: UniProtKB
- protein-containing complex binding Source: UniProtKB
- protein dimerization activity Source: InterPro
- RNA polymerase II cis-regulatory region sequence-specific DNA binding Source: GO_Central
GO - Biological processi
- cellular iron ion homeostasis Source: UniProtKB
- cellular response to DNA damage stimulus Source: UniProtKB
- chromatin remodeling Source: UniProtKB
- chromosome organization Source: UniProtKB
- MAPK cascade Source: UniProtKB
- negative regulation of apoptotic process Source: UniProtKB
- negative regulation of cell division Source: UniProtKB
- negative regulation of monocyte differentiation Source: UniProtKB
- negative regulation of stress-activated MAPK cascade Source: UniProtKB
- negative regulation of transcription by RNA polymerase II Source: GO_Central
- positive regulation of cell population proliferation Source: GO_Central
- positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
- positive regulation of DNA biosynthetic process Source: UniProtKB
- positive regulation of epithelial cell proliferation Source: UniProtKB
- positive regulation of fibroblast proliferation Source: UniProtKB
- positive regulation of response to DNA damage stimulus Source: UniProtKB
- positive regulation of transcription, DNA-templated Source: UniProtKB
- positive regulation of transcription by RNA polymerase II Source: UniProtKB
- regulation of somatic stem cell population maintenance Source: UniProtKB
- regulation of telomere maintenance Source: UniProtKB
- regulation of transcription, DNA-templated Source: UniProtKB
- response to drug Source: UniProtKB
- response to gamma radiation Source: UniProtKB
Keywordsi
Molecular function | Activator, DNA-binding |
Biological process | Transcription, Transcription regulation |
Names & Taxonomyi
Protein namesi | Recommended name: Myc proto-oncogene proteinAlternative name(s): Proto-oncogene c-Myc Transcription factor p64 |
Gene namesi | Name:MYC |
Organismi | Pan troglodytes (Chimpanzee) |
Taxonomic identifieri | 9598 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pan |
Proteomesi |
|
Subcellular locationi
Nucleus
- nucleoplasm By similarity
- nucleolus By similarity
Nucleus
- nucleolus Source: UniProtKB
- nucleoplasm Source: UniProtKB
- nucleus Source: UniProtKB
Keywords - Cellular componenti
NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000127297 | 1 – 439 | Myc proto-oncogene proteinAdd BLAST | 439 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 6 | PhosphoserineBy similarity | 1 | |
Modified residuei | 8 | PhosphothreonineBy similarity | 1 | |
Cross-linki | 52 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 58 | Phosphothreonine; by GSK3; alternateBy similarity | 1 | |
Glycosylationi | 58 | O-linked (GlcNAc) threonine; alternateBy similarity | 1 | |
Modified residuei | 62 | Phosphoserine; by DYRK2, GSK3 and CDK2By similarity | 1 | |
Modified residuei | 71 | PhosphoserineBy similarity | 1 | |
Modified residuei | 143 | N6-acetyllysine; by PCAF; alternateBy similarity | 1 | |
Cross-linki | 143 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity | ||
Modified residuei | 148 | N6-acetyllysine; alternateBy similarity | 1 | |
Cross-linki | 148 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity | ||
Modified residuei | 157 | N6-acetyllysine; by PCAFBy similarity | 1 | |
Modified residuei | 161 | PhosphoserineBy similarity | 1 | |
Modified residuei | 275 | N6-acetyllysine; by PCAFBy similarity | 1 | |
Modified residuei | 293 | PhosphoserineBy similarity | 1 | |
Cross-linki | 298 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 317 | N6-acetyllysine; by PCAFBy similarity | 1 | |
Modified residuei | 323 | N6-acetyllysine; by PCAFBy similarity | 1 | |
Modified residuei | 329 | Phosphoserine; by PIM2; in vitroBy similarity | 1 | |
Modified residuei | 371 | N6-acetyllysine; by PCAFBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | P23583 |
Interactioni
Subunit structurei
Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAX (By similarity).
Interacts with TAF1C and SPAG9.
Interacts with PARP10.
Interacts with KDM5A and KDM5B.
Interacts (when phosphorylated at Thr-58 and Ser-62) with FBXW7.
Interacts with PIM2.
Interacts with RIOX1. The heterodimer MYC:MAX interacts with ABI1; the interaction may enhance MYC:MAX transcriptional activity.
Interacts with TRIM6 (By similarity).
Interacts with NPM1; the binary complex is recruited to the promoter of MYC target genes and enhances their transcription (By similarity).
Interacts with CIP2A; leading to the stabilization of MYC (By similarity).
By similarityGO - Molecular functioni
- protein dimerization activity Source: InterPro
Protein-protein interaction databases
STRINGi | 9598.ENSPTRP00000035190 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 354 – 406 | bHLHPROSITE-ProRule annotationAdd BLAST | 53 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 413 – 434 | Leucine-zipperAdd BLAST | 22 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 33 – 37 | Poly-Gln | 5 | |
Compositional biasi | 88 – 91 | Poly-Gly | 4 |
Phylogenomic databases
eggNOGi | KOG2483, Eukaryota |
InParanoidi | P23583 |
Family and domain databases
CDDi | cd00083, HLH, 1 hit |
Gene3Di | 4.10.280.10, 1 hit |
InterProi | View protein in InterPro IPR011598, bHLH_dom IPR036638, HLH_DNA-bd_sf IPR003327, Myc-LZ IPR002418, Tscrpt_reg_Myc IPR012682, Tscrpt_reg_Myc_N |
Pfami | View protein in Pfam PF00010, HLH, 1 hit PF02344, Myc-LZ, 1 hit PF01056, Myc_N, 1 hit |
PIRSFi | PIRSF001705, Myc_protein, 1 hit |
PRINTSi | PR00044, LEUZIPPRMYC |
SMARTi | View protein in SMART SM00353, HLH, 1 hit |
SUPFAMi | SSF47459, SSF47459, 1 hit |
PROSITEi | View protein in PROSITE PS50888, BHLH, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MPLNVSFTNR NYDLDYDSVQ PYFYCDEEEN FYQQQQQSEL QPPAPSEDIW
60 70 80 90 100
KKFELLPTPP LSPSRRSGLC SPSYVAVTPF SLRGDNDGGG GSFSTADQLE
110 120 130 140 150
MVTELLGGDM VNQSFICDPD DETFIKNIII QDCMWSGFSA AAKLVSEKLA
160 170 180 190 200
SYQAARKDSG SPNPARGHSV CSTSSLYLQD LSAAASECID PSVVFPYPLN
210 220 230 240 250
DSSSPKSCPS QDSSAFSPSS DSLLSSTESS PQGSPEPLVL HEETPPTTSS
260 270 280 290 300
DSEEEQEDEE EIDVVSVEKR QAPGKRSESG SPSAGGHSKP PHSPLVLKRC
310 320 330 340 350
HVSTHQHNYA APPSTRKDYP AAKRVKLDSV RVLRQISNNR KCTSPRSSDT
360 370 380 390 400
EENDKRRTHN VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT
410 420 430
AYILSVQAEE QKLISEEDLL RKRREQLKHK LEQLRNSCA
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 202 | S → G in ABM91963 (Ref. 2) Curated | 1 | |
Sequence conflicti | 439 | A → V in ABM91963 (Ref. 2) Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M38057 Genomic DNA Translation: AAA72907.1 DQ977348 Genomic DNA Translation: ABM91963.1 AF519445 Genomic DNA Translation: AAN03870.1 |
PIRi | JU0449 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M38057 Genomic DNA Translation: AAA72907.1 DQ977348 Genomic DNA Translation: ABM91963.1 AF519445 Genomic DNA Translation: AAN03870.1 |
PIRi | JU0449 |
3D structure databases
BMRBi | P23583 |
SMRi | P23583 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 9598.ENSPTRP00000035190 |
Proteomic databases
PaxDbi | P23583 |
Phylogenomic databases
eggNOGi | KOG2483, Eukaryota |
InParanoidi | P23583 |
Family and domain databases
CDDi | cd00083, HLH, 1 hit |
Gene3Di | 4.10.280.10, 1 hit |
InterProi | View protein in InterPro IPR011598, bHLH_dom IPR036638, HLH_DNA-bd_sf IPR003327, Myc-LZ IPR002418, Tscrpt_reg_Myc IPR012682, Tscrpt_reg_Myc_N |
Pfami | View protein in Pfam PF00010, HLH, 1 hit PF02344, Myc-LZ, 1 hit PF01056, Myc_N, 1 hit |
PIRSFi | PIRSF001705, Myc_protein, 1 hit |
PRINTSi | PR00044, LEUZIPPRMYC |
SMARTi | View protein in SMART SM00353, HLH, 1 hit |
SUPFAMi | SSF47459, SSF47459, 1 hit |
PROSITEi | View protein in PROSITE PS50888, BHLH, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | MYC_PANTR | |
Accessioni | P23583Primary (citable) accession number: P23583 Secondary accession number(s): A2T708, Q8MJ74 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1991 |
Last sequence update: | November 1, 1991 | |
Last modified: | December 2, 2020 | |
This is version 148 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |